Purification of viral proteins from avian sarcoma virus QV2

A procedure was established whereby most of the major viral proteins were isolated to apparent homogeneity in biologically and immunologically active forms from a single batch of avian sarcoma virus QV2. For the initial step of purification, gently disrupted virions were fractionated by CsCl centrif...

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Published in:Journal of biochemistry (Tokyo) 1979-01, Vol.86 (4), p.929-942
Main Authors: UENO, Akemichi, KOHNO, Michiaki, ISHIHAMA, Akira, TOYOSHIMA, Kumao
Format: Article
Language:English
Subjects:
DNA-Directed DNA Polymerase - isolation & purification
Immunodiffusion
Membrane Proteins - isolation & purification
Molecular Weight
Retroviridae - analysis
Retroviridae - enzymology
Viral Proteins - isolation & purification
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container_title Journal of biochemistry (Tokyo)
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creator UENO, Akemichi
KOHNO, Michiaki
ISHIHAMA, Akira
TOYOSHIMA, Kumao
description A procedure was established whereby most of the major viral proteins were isolated to apparent homogeneity in biologically and immunologically active forms from a single batch of avian sarcoma virus QV2. For the initial step of purification, gently disrupted virions were fractionated by CsCl centrifugation into envelope proteins, RNA-dependent DNA polymerase, and viral core proteins. Further purification of envelope glycoproteins and DNA polymerase was performed by affinity chromatography on agarose columns cross-linked with plant lectins and poly(C), respectively. On the other hand, core proteins were fractionated by a combination of gel filtration and ion-exchange column chromatography into components p27, pl9, and p15. The core protein p15 thus isolated retained proteolytic activity even after storage for 6 months. The present study also demonstrated that QV2 p19 is structurally altered from the corresponding protein of avian myeloblastosis virus (AMV), a reference avian leukosis-sarcoma virus having a well-characterized polypeptide composition.
doi_str_mv 10.1093/oxfordjournals.jbchem.a132625
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source J-STAGE (Japan Science & Technology Information Aggregator, Electronic) - Open Access English articles; Oxford University Press Archive
subjects DNA-Directed DNA Polymerase - isolation & purification
Immunodiffusion
Membrane Proteins - isolation & purification
Molecular Weight
Retroviridae - analysis
Retroviridae - enzymology
Viral Proteins - isolation & purification
title Purification of viral proteins from avian sarcoma virus QV2
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